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Evaluation of the prostaglandin F synthase activity of human and bovine aldo-keto reductases: AKR1A1s complement AKR1B1s as potent PGF synthases.

Authors: Lacroix Pepin, N  Chapdelaine, P  Fortier, MA 
Citation: Lacroix Pepin N, etal., Prostaglandins Other Lipid Mediat. 2013 Oct;106:124-32. doi: 10.1016/j.prostaglandins.2013.05.005. Epub 2013 Jun 6.
Pubmed: (View Article at PubMed) PMID:23747692
DOI: Full-text: DOI:10.1016/j.prostaglandins.2013.05.005

AKR1B1 of the polyol pathway was identified as a prostaglandin F2alpha synthase (PGFS). Using a genomic approach we have identified in the endometrium five bovine and three human AKRs with putative PGFS activity and generated the corresponding recombinant enzymes. The PGFS activity of the recombinant proteins was evaluated using a novel assay based on in situ generation of the precursor of PG biosynthesis PGH2. PGF2alpha was measured by ELISA and the relative potencies of the different enzymes were compared. We identified AKR1A1 and confirmed AKR1B1 as the most potent PGFS expressing characteristic inhibition patterns in presence of methylglyoxal, ponalrestat and glucose.

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RGD Object Information
RGD ID: 8552778
Created: 2014-04-28
Species: All species
Last Modified: 2014-04-28
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.